Evidence map›Paper›PMID 32001694›Full record

ArticleNature communications2020

Structural basis for electron transport mechanism of complex I-like photosynthetic NAD(P)H dehydrogenase.

Xiaowei Pan, Duanfang Cao, Fen Xie, Fang Xu, Xiaodong Su, Hualing Mi, Xinzheng Zhang, Mei Li

Open access · greenAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
3.6field-weighted citation impact, top 6% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

48 citing papers in PubMed, 49 citations in OpenAlex.

  1. OsRNase ZPlant communications · 2026
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  7. Action at a distance: The remarkable coupling of COProceedings of the National Academy of Sciences of the United States of America · 2025
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  15. Unique structural attributes of the PSI-NDH supercomplex in Physcomitrium patens.The Plant journal : for cell and molecular biology · 2024
    Article
  16. DIA-Based Quantitative Proteomics in the Flower Buds of TwoInternational journal of molecular sciences · 2024
    Article
  17. Article
  18. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 4 institutions in 1 country.

Xiaowei Pan *National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, PR China.ORCID http://orcid.org/0000-0002-9672-4649
Duanfang Cao *National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, PR China.ORCID http://orcid.org/0000-0002-1229-3950
Fen Xie *National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, PR China.
Fang Xu *University of Chinese Academy of Sciences, Beijing, 100049, PR China.
Xiaodong SuNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, PR China.
Hualing MiNational Key Laboratory of Plant Molecular Genetics, Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences, Chinese Academy of Science, Shanghai, 200032, PR China. hlmi@sibs.ac.cn.
Xinzheng ZhangNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, PR China. xzzhang@ibp.ac.cn.ORCID http://orcid.org/0000-0002-0114-0270
Mei LiNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, PR China. meili@ibp.ac.cn.ORCID http://orcid.org/0000-0002-1742-2360
Institute of Biophysics · CNCenter for Excellence in Molecular Plant Sciences · CNChinese Academy of Sciences · CNUniversity of Chinese Academy of Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

NAD(P)H dehydrogenase-like (NDH) complex NDH-1L of cyanobacteria plays a crucial role in cyclic electron flow (CEF) around photosystem I and respiration processes. NDH-1L couples the electron transport from ferredoxin (Fd) to plastoquinone (PQ) and proton pumping from cytoplasm to the lumen that drives the ATP production. NDH-1L-dependent CEF increases the ATP/NADPH ratio, and is therefore pivotal for oxygenic phototrophs to function under stress. Here we report two structures of NDH-1L from Thermosynechococcus elongatus BP-1, in complex with one Fd and an endogenous PQ, respectively. Our structures represent the complete model of cyanobacterial NDH-1L, revealing the binding manner of NDH-1L with Fd and PQ, as well as the structural elements crucial for proper functioning of the NDH-1L complex. Together, our data provides deep insights into the electron transport from Fd to PQ, and its coupling with proton translocation in NDH-1L.

Indexed as

PhotosynthesisBinding SitesCarotenoidsCell MembraneElectron TransportElectron Transport Complex IFerredoxinsHydrophobic and Hydrophilic InteractionsLipidsModels, MolecularNADPH DehydrogenasePlastoquinoneProtein DomainsProtein SubunitsStructural Homology, ProteinThermusCarotenoidsElectron Transport Complex IFerredoxinsLipidsNADPH DehydrogenasePlastoquinoneProtein Subunits

Identifiers

PMID32001694
PMCPMC6992706
OpenAlexW3004385852

What OpenQuestion holds

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LicenceCC BY
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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.